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339205-36-6

(Z-L-Cys-DL-ValOMe)2 is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

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  • 339205-36-6 Structure

  • Basic information

    1. Product Name: (Z-L-Cys-DL-ValOMe)2
    2. Synonyms: (Z-L-Cys-DL-ValOMe)2
    3. CAS NO:339205-36-6
    4. Molecular Formula:
    5. Molecular Weight: 734.892
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 339205-36-6.mol

  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: N/A
    3. Flash Point: N/A
    4. Appearance: N/A
    5. Density: N/A
    6. Refractive Index: N/A
    7. Storage Temp.: N/A
    8. Solubility: N/A
    9. CAS DataBase Reference: (Z-L-Cys-DL-ValOMe)2(CAS DataBase Reference)
    10. NIST Chemistry Reference: (Z-L-Cys-DL-ValOMe)2(339205-36-6)
    11. EPA Substance Registry System: (Z-L-Cys-DL-ValOMe)2(339205-36-6)

  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 339205-36-6(Hazardous Substances Data)

339205-36-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 339205-36-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 3,3,9,2,0 and 5 respectively; the second part has 2 digits, 3 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 339205-36:
(8*3)+(7*3)+(6*9)+(5*2)+(4*0)+(3*5)+(2*3)+(1*6)=136
136 % 10 = 6
So 339205-36-6 is a valid CAS Registry Number.

339205-36-6Downstream Products

339205-36-6Relevant articles and documents

Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase

Bounaga, Sakina,Galleni, Moreno,Laws, Andrew P,Page, Michael I

, p. 503 - 510 (2007/10/03)

Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site.

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